TreSA (PP_2918) is a standalone glycoside-hydrolase-family TreS enzyme that reversibly interconverts D-maltose and alpha,alpha-trehalose. Recombinant KT2440 TreS has been shown to form trehalose from maltose in vitro; the physiological direction and contribution of PP_2918 in native KT2440 cells remain unresolved.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0047471 maltose alpha-D-glucosyltransferase activity | IEA GO_REF:0000003 | ACCEPT | Summary: TreSA catalyzes the reversible EC 5.4.99.16 interconversion of maltose and alpha,alpha-trehalose. Reason: Q88IT1 carries the Pseudomonas-type TreS signatures (TIGR02455, IPR012665) shared with the characterized P. stutzeri CJ38 TreS. Recombinant TreS cloned from P. putida KT2440 converted maltose to trehalose by HPLC, directly supporting the annotated molecular function. The PubMed abstract does not name PP_2918, but the N-terminal cloning primer reported in the companion full article encodes the exact Q88IT1 N terminus. The abstract's reported 67-kDa mass conflicts with the companion article's approximately 76-kDa value and matches neither KT2440 candidate; this identity limitation is documented in treSA-notes.md. Supporting Evidence: file:PSEPK/treSA/treSA-uniprot.txt DR NCBIfam; TIGR02455; TreS_stutzeri; 1. file:PSEPK/treSA/treSA-uniprot.txt DR InterPro; IPR012665; Trehalose_synth. PMID:25204684 High-pressure liquid chromatography results indicated that this enzyme had the ability to catalyze 59% maltose into trehalose, with about 5.1% glucose as by-product. |
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Download this section (compressed HTML)Q: Under which carbon-source or osmotic-stress conditions does native KT2440 route flux through TreSA rather than TreY-TreZ or TreSB?
Experiment: Quantify maltose, trehalose, and alpha-glucan in wild type and single and combined treSA, treY-treZ, and treSB mutants across carbon and osmotic-stress conditions.
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